Structure analysis

STRUCTURE OF CAMP-DEPENDENT PROTEIN KINASE, ALPHA-CATALYTIC SUBUNIT IN COMPLEX WITH H89 PROTEIN KINASE INHIBITOR N-[2-(4-BROMOCINNAMYLAMINO)ETHYL]-5-ISOQUINOLINE

X-ray diffraction
2.3Å resolution
Source organisms:
Assembly composition:
hetero dimer (preferred)
Entry contents: 2 distinct polypeptide molecules

Assemblies

Assembly 1 (preferred)
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Multimeric state: hetero dimer
Accessible surface area: 15700 Å2
Buried surface area: 2900 Å2
Dissociation area: 1,400 Å2
Dissociation energy (ΔGdiss): -2 kcal/mol
Dissociation entropy (TΔSdiss): 10 kcal/mol
Interface energy (ΔGint): 2 kcal/mol
Symmetry number: 1

Macromolecules

Chain: E
Length: 350 amino acids
Theoretical weight: 40.68 KDa
Source organism: Bos taurus
Expression system: Escherichia coli
UniProt:
  • Canonical: P00517 (Residues: 2-351; Coverage: 100%)
Gene name: PRKACA
Pfam: Protein kinase domain
InterPro:
CATH:
SCOP: Protein kinases, catalytic subunit

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Chain: I
Length: 20 amino acids
Theoretical weight: 2.23 KDa
Source organism: Rattus norvegicus
Expression system: Not provided
UniProt:
  • Canonical: P63249 (Residues: 6-25; Coverage: 26%)
Gene name: Pkia
InterPro: cAMP-dependent protein kinase inhibitor

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